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BPHS2_PICSI
ID   BPHS2_PICSI             Reviewed;         624 AA.
AC   C0PTH8;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=(-)-beta-phellandrene synthase 2, chloroplastic {ECO:0000303|PubMed:21385377};
DE            EC=4.2.3.52 {ECO:0000269|PubMed:21385377};
DE   AltName: Full=Terpene synthase TPS-Phel-2 {ECO:0000303|PubMed:21385377};
DE            Short=PsTPS-Phel-2 {ECO:0000303|PubMed:21385377};
DE   Flags: Precursor;
GN   Name=TPS-Phel-2 {ECO:0000303|PubMed:21385377};
OS   Picea sitchensis (Sitka spruce) (Pinus sitchensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX   NCBI_TaxID=3332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. FB3-425; TISSUE=Bark;
RX   PubMed=18854048; DOI=10.1186/1471-2164-9-484;
RA   Ralph S.G., Chun H.J.E., Kolosova N., Cooper D., Oddy C., Ritland C.E.,
RA   Kirkpatrick R., Moore R., Barber S., Holt R.A., Jones S.J.M., Marra M.A.,
RA   Douglas C.J., Ritland K., Bohlmann J.;
RT   "A conifer genomics resource of 200,000 spruce (Picea spp.) ESTs and 6,464
RT   high-quality, sequence-finished full-length cDNAs for Sitka spruce (Picea
RT   sitchensis).";
RL   BMC Genomics 9:484-484(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, PATHWAY, AND GENE
RP   FAMILY.
RC   STRAIN=cv. FB3-425;
RX   PubMed=21385377; DOI=10.1186/1471-2229-11-43;
RA   Keeling C.I., Weisshaar S., Ralph S.G., Jancsik S., Hamberger B.,
RA   Dullat H.K., Bohlmann J.;
RT   "Transcriptome mining, functional characterization, and phylogeny of a
RT   large terpene synthase gene family in spruce (Picea spp.).";
RL   BMC Plant Biol. 11:43-43(2011).
CC   -!- FUNCTION: Terpene synthase (TPS) involved in the biosynthesis of
CC       monoterpene natural products included in conifer oleoresin secretions
CC       and volatile emissions; these compounds contribute to biotic and
CC       abiotic stress defense against herbivores and pathogens
CC       (PubMed:21385377). Catalyzes the conversion of (2E)-geranyl diphosphate
CC       (GPP) to (-)-beta-phellandrene (PubMed:21385377).
CC       {ECO:0000269|PubMed:21385377}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate = (-)-beta-phellandrene +
CC         diphosphate; Xref=Rhea:RHEA:25492, ChEBI:CHEBI:129,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.52;
CC         Evidence={ECO:0000269|PubMed:21385377};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC       Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC       {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC   -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC       {ECO:0000269|PubMed:21385377}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC   -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC       the catalytic activity, presumably through binding to Mg(2+).
CC       {ECO:0000250|UniProtKB:A0A1C9J6A7}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BT071667; ACN41118.1; -; mRNA.
DR   EMBL; HQ426169; ADZ45506.1; -; mRNA.
DR   BRENDA; 4.2.3.52; 8974.
DR   UniPathway; UPA00924; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0016829; F:lyase activity; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR   GO; GO:0010597; P:green leaf volatile biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0016099; P:monoterpenoid biosynthetic process; IDA:UniProtKB.
DR   CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR   Gene3D; 1.10.600.10; -; 1.
DR   Gene3D; 1.50.10.130; -; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR034741; Terpene_cyclase-like_1_C.
DR   InterPro; IPR044814; Terpene_cyclase_plant_C1.
DR   InterPro; IPR001906; Terpene_synth_N.
DR   InterPro; IPR036965; Terpene_synth_N_sf.
DR   InterPro; IPR005630; Terpene_synthase_metal-bd.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   Pfam; PF01397; Terpene_synth; 1.
DR   Pfam; PF03936; Terpene_synth_C; 1.
DR   SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR   SUPFAM; SSF48239; SSF48239; 1.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT   TRANSIT         1..48
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           49..624
FT                   /note="(-)-beta-phellandrene synthase 2, chloroplastic"
FT                   /id="PRO_0000454405"
FT   MOTIF           375..379
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         375
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         375
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         379
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         379
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         527
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
SQ   SEQUENCE   624 AA;  71427 MW;  0CA88833C6A66302 CRC64;
     MAIVSSVPLA SKSCLHKSLI SSIHKLKPFC RTIPTLGMSR PGKYVMPSMS MSSPVSDDGV
     QRRTGGYHSN LWNDDIIQFL STTYGEPAYR ERGERLIDEV KNMFNSISME DVEFSPLNDL
     IQRLWIVDSV ERLGIDRHFK NEIKSTLDYV YSYWTQKGIG CGIESVVPDL NSTALGLRTL
     RLHGYPVSAE VLKHFQNQNG QFACSPSETE GEMRSIVNLY RASLIAFPGE KVMEEAEIFS
     TKYLKEALQK IPVSSLSREI GDVLEQDWHT NLPRLEARNY IDVFGQDTKD TKLYMKTEKL
     LELAKLEFNI FQSLQKTELD SLLRWWKDSG FHHITFSRHL HVEYYTLASC IAIEPQHSRF
     RLGFAKACHV ITILDDMYDV FGTIDELELF TAQIKRWDPS ATDCLPKYMK RMYMILYDMV
     NEMSREAETA QGRDTLNYAR QAWEDFIDSY MQEAKWIATG YLPTFDEYFE NGKVSSGHRV
     AALQPILTMD IPFPHDILKE VDFPSKLNDL ASAILRLRGD TRCYKADRAR GEEASCISCY
     MKDNPGATEE DALSHINAVI SDVIKGLNWE LLNPNSSVPI SSKKHVFDVS RALHYGYKYR
     DGYSVSNIET KSLVMRTLLE SVPF
 
 
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